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  Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.

Colbert, K. N., Hattendorf, D. A., Weiss, T. M., Burkhardt, P., Fasshauer, D., & Weis, W. I. (2013). Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation. Proceedings of the National Academy of Sciences of the United States of America, 110(31), 12637-12642. doi:10.1073/pnas.1303753110.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-4CB9-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-80F0-3
Genre: Journal Article

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Colbert, K. N., Author
Hattendorf, D. A., Author
Weiss, T. M., Author
Burkhardt, P.1, Author              
Fasshauer, D.1, Author              
Weis, W. I., Author
Affiliations:
1Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578596              

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 Abstract: In neurons, soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1-24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1a Delta N), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1a Delta N, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a-Syx1a complex.

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Language(s): eng - English
 Dates: 2013-07-152013-07-30
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1303753110
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 110 (31) Sequence Number: - Start / End Page: 12637 - 12642 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230